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| | ==Crystal structure of RoqN== | | ==Crystal structure of RoqN== |
| - | <StructureSection load='5w7m' size='340' side='right' caption='[[5w7m]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5w7m' size='340' side='right'caption='[[5w7m]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w7m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_rubens_Wisconsin_54-1255 Penicillium rubens Wisconsin 54-1255]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W7M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7m OCA], [http://pdbe.org/5w7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7m RCSB], [http://www.ebi.ac.uk/pdbsum/5w7m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7m ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7m OCA], [https://pdbe.org/5w7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w7m RCSB], [https://www.ebi.ac.uk/pdbsum/5w7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ROQN_PENRW ROQN_PENRW]] Glandicoline B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin meleagrin (PubMed:22118684, PubMed:23776469). The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (PubMed:22118684, PubMed:23776469). HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469). In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469). In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469). Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469). Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469). More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).<ref>PMID:22118684</ref> <ref>PMID:23776469</ref> <ref>PMID:24225953</ref> | + | [https://www.uniprot.org/uniprot/ROQN_PENRW ROQN_PENRW] Glandicoline B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin meleagrin (PubMed:22118684, PubMed:23776469). The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (PubMed:22118684, PubMed:23776469). HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469). In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469). In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469). Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469). Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469). More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).<ref>PMID:22118684</ref> <ref>PMID:23776469</ref> <ref>PMID:24225953</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Berlinck, R G.S]] | + | [[Category: Large Structures]] |
| - | [[Category: Newmister, S A]] | + | [[Category: Penicillium rubens Wisconsin 54-1255]] |
| - | [[Category: Romminger, S]] | + | [[Category: Berlinck RGS]] |
| - | [[Category: Schmidt, J J]] | + | [[Category: Newmister SA]] |
| - | [[Category: Sherman, D H]] | + | [[Category: Romminger S]] |
| - | [[Category: Smith, J L]] | + | [[Category: Schmidt JJ]] |
| - | [[Category: Williams, R M]] | + | [[Category: Sherman DH]] |
| - | [[Category: Hydrolase]] | + | [[Category: Smith JL]] |
| - | [[Category: Indole alkaloid]] | + | [[Category: Williams RM]] |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Oxaline]]
| + | |
| - | [[Category: Penicillium chrysogenum]]
| + | |
| Structural highlights
Function
ROQN_PENRW Glandicoline B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin meleagrin (PubMed:22118684, PubMed:23776469). The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (PubMed:22118684, PubMed:23776469). HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469). In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469). In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469). Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469). Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469). More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).[1] [2] [3]
References
- ↑ Garcia-Estrada C, Ullan RV, Albillos SM, Fernandez-Bodega MA, Durek P, von Dohren H, Martin JF. A single cluster of coregulated genes encodes the biosynthesis of the mycotoxins roquefortine C and meleagrin in Penicillium chrysogenum. Chem Biol. 2011 Nov 23;18(11):1499-512. doi: 10.1016/j.chembiol.2011.08.012. PMID:22118684 doi:http://dx.doi.org/10.1016/j.chembiol.2011.08.012
- ↑ Ali H, Ries MI, Nijland JG, Lankhorst PP, Hankemeier T, Bovenberg RA, Vreeken RJ, Driessen AJ. A branched biosynthetic pathway is involved in production of roquefortine and related compounds in Penicillium chrysogenum. PLoS One. 2013 Jun 12;8(6):e65328. doi: 10.1371/journal.pone.0065328. Print 2013. PMID:23776469 doi:http://dx.doi.org/10.1371/journal.pone.0065328
- ↑ Ries MI, Ali H, Lankhorst PP, Hankemeier T, Bovenberg RA, Driessen AJ, Vreeken RJ. Novel key metabolites reveal further branching of the roquefortine/meleagrin biosynthetic pathway. J Biol Chem. 2013 Dec 27;288(52):37289-95. doi: 10.1074/jbc.M113.512665. Epub, 2013 Nov 13. PMID:24225953 doi:http://dx.doi.org/10.1074/jbc.M113.512665
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